Calcium-binding EGF-like modules in coagulation proteinases: function of the calcium ion in module interactions.
暂无分享,去创建一个
[1] E. Thulin,et al. EGF-like module pair 3-4 in vitamin K-dependent protein S: modulation of calcium affinity of module 4 by module 3, and interaction with factor X. , 1999, Journal of molecular biology.
[2] T. Darden,et al. Probing the structural changes in the light chain of human coagulation factor VIIa due to tissue factor association. , 1999, Biophysical journal.
[3] R. Kelley,et al. The effect of O-fucosylation on the first EGF-like domain from human blood coagulation factor VII. , 1999, Biochemistry.
[4] A. Holder,et al. Solution structure of an EGF module pair from the Plasmodium falciparum merozoite surface protein 1. , 1999, Journal of molecular biology.
[5] S. Artavanis-Tsakonas,et al. Notch signaling: cell fate control and signal integration in development. , 1999, Science.
[6] N. Thielens,et al. The N-terminal CUB-Epidermal Growth Factor Module Pair of Human Complement Protease C1r Binds Ca2+ with High Affinity and Mediates Ca2+-dependent Interaction with C1s* , 1999, The Journal of Biological Chemistry.
[7] P. Handford,et al. EGF-like domain calcium affinity modulated by N-terminal domain linkage in human fibrillin-1. , 1999, Journal of molecular biology.
[8] P. Handford,et al. Defective calcium binding to fibrillin-1: consequence of an N2144S change for fibrillin-1 structure and function. , 1999, Journal of molecular biology.
[9] S. Kent,et al. Chemical synthesis of human protein S thrombin-sensitive module and first epidermal growth factor module. , 1998, Biopolymers.
[10] G. Gippert,et al. Solution structure of the N-terminal EGF-like domain from human factor VII. , 1998, Biochemistry.
[11] I. Campbell,et al. NMR of modular proteins , 1998, Nature Structural Biology.
[12] P. Handford,et al. A Gly → Ser Change Causes Defective Folding in Vitro of Calcium-binding Epidermal Growth Factor-like Domains from Factor IX and Fibrillin-1* , 1998, The Journal of Biological Chemistry.
[13] D. Marion,et al. Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family. , 1998, Biochemistry.
[14] B. Dahlbäck,et al. Characterization of recombinant epidermal growth factor (EGF)-like modules from vitamin-K-dependent protein S expressed in Spodoptera cells--the cofactor activity depends on the N-terminal EGF module in human protein S. , 1998, European journal of biochemistry.
[15] O. Christophe,et al. Blood Coagulation Factor IX Residues Glu78 and Arg94 Provide a Link between Both Epidermal Growth Factor-like Domains That Is Crucial in the Interaction with Factor VIII Light Chain* , 1998, The Journal of Biological Chemistry.
[16] B. Villoutreix,et al. Calcium binding to tandem repeats of EGF‐like modules. Expression and characterization of the EGF‐like modules of human Notch‐1 implicated in receptor‐ligand interactions , 1997, Protein science : a publication of the Protein Society.
[17] S. Linse,et al. The High Affinity Calcium-binding Sites in the Epidermal Growth Factor Module Region of Vitamin K-dependent Protein S* , 1997, The Journal of Biological Chemistry.
[18] T. Drakenberg,et al. Calcium-binding properties of the third and fourth epidermal-growth-factor-like modules in vitamin-K-dependent protein S. , 1997, European journal of biochemistry.
[19] W. Ruf,et al. Ca2+ Binding to the First Epidermal Growth Factor Module of Coagulation Factor VIIa Is Important for Cofactor Interaction and Proteolytic Function* , 1997, The Journal of Biological Chemistry.
[20] T. Edgington,et al. The Structural Basis of Function of the TF●VIIa Complex in the Cellular Initiation of Coagulation , 1997, Thrombosis and Haemostasis.
[21] S Foundling,et al. The 2.8 A crystal structure of Gla‐domainless activated protein C. , 1996, The EMBO journal.
[22] J. Trewhella,et al. The relative orientation of Gla and EGF domains in coagulation factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study. , 1996, Biochemistry.
[23] I. Campbell,et al. Solution Structure of a Pair of Calcium-Binding Epidermal Growth Factor-like Domains: Implications for the Marfan Syndrome and Other Genetic Disorders , 1996, Cell.
[24] P Bork,et al. Structure and distribution of modules in extracellular proteins , 1996, Quarterly Reviews of Biophysics.
[25] David W. Banner,et al. The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor , 1996, Nature.
[26] P. Handford,et al. Calcium binding properties of an epidermal growth factor-like domain pair from human fibrillin-1. , 1996, Journal of molecular biology.
[27] P. Handford,et al. The structure of a Ca2+-binding epidermal growth factor-like domain: Its role in protein-protein interactions , 1995, Cell.
[28] S. Forsén,et al. Structure of the Ca2+-free GLA domain sheds light on membrane binding of blood coagulation proteins , 1995, Nature Structural Biology.
[29] P. Handford,et al. The Calcium Binding Properties and Molecular Organization of Epidermal Growth Factor-like Domains in Human Fibrillin-1 (*) , 1995, The Journal of Biological Chemistry.
[30] R. Glanville,et al. Calcium binding, hydroxylation, and glycosylation of the precursor epidermal growth factor-like domains of fibrillin-1, the Marfan gene protein. , 1994, The Journal of biological chemistry.
[31] A. Holmgren,et al. Calcium-dependent interaction between gamma-carboxyglutamic acid-containing and N-terminal epidermal growth factor-like modules in factor X. , 1994, The Journal of biological chemistry.
[32] M. Ullner,et al. How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in coagulation factor X. , 1994, The Journal of biological chemistry.
[33] P. Loll,et al. The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1 , 1994, Nature.
[34] C. Kielty,et al. The role of calcium in the organization of fibrillin microfibrils , 1993, FEBS letters.
[35] J. Stenflo,et al. Calcium affinity of the NH2-terminal epidermal growth factor-like module of factor X. Effect of the gamma-carboxyglutamic acid-containing module. , 1993, The Journal of biological chemistry.
[36] I. Campbell,et al. The effect of aspartate hydroxylation on calcium binding to epidermal growth factor-like modules in coagulation factors IX and X. , 1993, The Journal of biological chemistry.
[37] P. Handford,et al. Tyrosine 69 of the first epidermal growth factor-like domain of human factor IX is essential for clotting activity. , 1993, The Journal of biological chemistry.
[38] R. Huber,et al. Structure of human des(1-45) factor Xa at 2.2 A resolution. , 1993, Journal of molecular biology.
[39] R F Doolittle,et al. The Evolution of Vertebrate Blood Coagulation: A Case of Yin and Yang , 1993, Thrombosis and Haemostasis.
[40] P. Bork,et al. Epidermal growth factor-like modules , 1993 .
[41] Reed J. Harris,et al. O-linked fucose and other post-translational modifications unique to EGF modules. , 1993, Glycobiology.
[42] K. O. Elliston,et al. cDNA cloning and expression of bovine aspartyl (asparaginyl) beta-hydroxylase. , 1992, The Journal of biological chemistry.
[43] T. Drakenberg,et al. Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding. , 1992, Biochemistry.
[44] C. Esmon,et al. The high affinity calcium-binding site involved in protein C activation is outside the first epidermal growth factor homology domain. , 1992, The Journal of biological chemistry.
[45] I. Campbell,et al. Solution structure of the fifth repeat of factor H: a second example of the complement control protein module. , 1992, Biochemistry.
[46] I. Campbell,et al. The three‐dimensional structure of the first EGF‐like module of human factor IX: Comparison with EGF and TGF‐α , 1992, Protein science : a publication of the Protein Society.
[47] G. Long,et al. beta-Hydroxyaspartic acid and beta-hydroxyasparagine residues in recombinant human protein S are not required for anticoagulant cofactor activity or for binding to C4b-binding protein. , 1991, The Journal of biological chemistry.
[48] J. Stenflo,et al. Structure-function relationships of epidermal growth factor modules in vitamin K-dependent clotting factors. , 1991, Blood.
[49] R. Glanville,et al. Partial sequence of a candidate gene for the Marfan syndrome , 1991, Nature.
[50] M. Mattei,et al. Linkage of Marfan syndrome and a phenotypically related disorder to two different fibrillin genes , 1991, Nature.
[51] W. Kisiel,et al. Human plasma and recombinant factor VII. Characterization of O-glycosylations at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine. , 1991, The Journal of biological chemistry.
[52] László Patthy,et al. Modular exchange principles in proteins , 1991 .
[53] I. D. Campbell,et al. Key residues involved in calcium-binding motifs in EGF-like domains , 1991, Nature.
[54] J. Stenflo,et al. Protein structural requirements for Ca2+ binding to the light chain of factor X. Studies using isolated intact fragments containing the gamma-carboxyglutamic acid region and/or the epidermal growth factor-like domains. , 1991, The Journal of biological chemistry.
[55] B. Dahlbäck,et al. Novel type of very high affinity calcium-binding sites in beta-hydroxyasparagine-containing epidermal growth factor-like domains in vitamin K-dependent protein S. , 1990, The Journal of biological chemistry.
[56] J. Stenflo,et al. sup 1 H NMR assignment and secondary structure of the Ca sup 2+ -free form of the amino-terminal epidermal growth factor like domain in coagulation factor X , 1990 .
[57] D. Monroe,et al. Characterization of the functional defect in factor IX Alabama. Evidence for a conformational change due to high affinity calcium binding in the first epidermal growth factor domain. , 1990, The Journal of biological chemistry.
[58] V. Garsky,et al. Partial purification and characterization of bovine liver aspartyl beta-hydroxylase. , 1990, The Journal of biological chemistry.
[59] W. Kisiel,et al. Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z. , 1989, The Journal of biological chemistry.
[60] S. Linse,et al. Calcium binding to the isolated beta-hydroxyaspartic acid-containing epidermal growth factor-like domain of bovine factor X. , 1989, The Journal of biological chemistry.
[61] J. Engel. EGF‐like domains in extracellular matrix proteins: Localized signals for growth and differentiation? , 1989, FEBS letters.
[62] K. Berkner,et al. Inhibitors of 2-ketoglutarate-dependent dioxygenases block aspartyl beta-hydroxylation of recombinant human factor IX in several mammalian expression systems. , 1989, The Journal of biological chemistry.
[63] S. Kawabata,et al. A new trisaccharide sugar chain linked to a serine residue in bovine blood coagulation factors VII and IX. , 1988, Journal of biochemistry.
[64] L. Thim,et al. Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells. , 1988, Biochemistry.
[65] P. Handford,et al. The role of beta‐hydroxyaspartate and adjacent carboxylate residues in the first EGF domain of human factor IX. , 1988, The EMBO journal.
[66] S. Linse,et al. Calcium binding to the epidermal growth factor homology region of bovine protein C. , 1988, The Journal of biological chemistry.
[67] B. Furie,et al. The molecular basis of blood coagulation , 1988, Cell.
[68] W. Schneider,et al. beta-Hydroxyaspartic acid or beta-hydroxyasparagine in bovine low density lipoprotein receptor and in bovine thrombomodulin. , 1988, The Journal of biological chemistry.
[69] J. Stenflo,et al. Calcium-dependent interaction between the epidermal growth factor precursor-like region of human protein C and a monoclonal antibody. , 1987, The Journal of biological chemistry.
[70] C. Esmon,et al. The active site of blood coagulation factor Xa. Its distance from the phospholipid surface and its conformational sensitivity to components of the prothrombinase complex. , 1987, The Journal of biological chemistry.
[71] Richard G. W. Anderson,et al. Acid-dependent ligand dissociation and recycling of LDL receptor mediated by growth factor homology region , 1987, Nature.
[72] F. Blasi,et al. Urokinase-type plasminogen activator: proenzyme, receptor, and inhibitors , 1987, The Journal of cell biology.
[73] L. Patthy. Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules , 1985, Cell.
[74] T. Südhof,et al. The LDL receptor gene: a mosaic of exons shared with different proteins. , 1985, Science.
[75] P. Fernlund,et al. β‐Hydroxyaspartic acid in vitamin K‐dependent plasma proteins from scorbutic and warfarin‐treated guinea pigs , 1984 .
[76] P. Fernlund,et al. Beta-hydroxyaspartic acid in vitamin K-dependent proteins. , 1983, The Journal of biological chemistry.
[77] A. M. Soderquist,et al. EPIDERMAL GROWTH FACTOR * , 1982, Annals of the New York Academy of Sciences.
[78] Kenji Matsuno,et al. Notch signaling. , 1995, Science.
[79] L. Patthy. Modular design of proteases of coagulation, fibrinolysis, and complement activation: implications for protein engineering and structure-function studies. , 1993, Methods in enzymology.
[80] J. Astermark,et al. Isolation of intact modules from noncatalytic parts of vitamin K-dependent coagulation factors IX and X and protein C. , 1993, Methods in enzymology.
[81] I. Campbell,et al. The solution structure of human epidermal growth factor , 1987, Nature.
[82] J. Ware,et al. Factor IXAlabama: a point mutation in a clotting protein results in hemophilia B. , 1987, Blood.